P21550 (ENOB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-enolase
EC=4.2.1.11

Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 3
Muscle-specific enolase
Short name=MSE
Skeletal muscle enolase

Gene names

Name:	Eno3
Synonyms:	Eno-3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Appears to have a function in striated muscle development and regeneration.
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H2O.
Cofactor	Magnesium. Required for catalysis and for stabilizing the dimer.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subunit structure	Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. In vitro, interacts with several glycolytic enzymes including PKM, PGM, CKM and ALDO. Also binds PLG and troponin, in vitro. Interacts with PNKD By similarity. Ref.9
Subcellular location	Cytoplasm. Note: Localized to the Z line. Some colocalization with CKM at M-band By similarity. Ref.10
Tissue specificity	The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. In striated muscle, the fiber-type order of ENO3 expression is IIB > IIX > IIA > I. Ref.10
Developmental stage	During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells, and to the alpha/gamma heterodimer in nerve cells. In hindleg muscle, first expressed at E15 after which, levels increase sharply between E15 and E17. A steep prenatal rise in expression accompanies the formation of secondary myofibers and the development of innervation. High levels continue throughout newborn and adult stages. Beginning at postnatal day 5, a second sharp increase in expression correlates with the definitive specialization of the myofibers. Later in development, mainly expressed in fast-twitch fibers. In cardiac muscle, first expressed in the embryo in the cardiac tube. Ref.8 Ref.9
Induction	Levels decrease in degenerating myofibers, and increase with their regeneration. Ref.11
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from electronic annotation. Source: Compara glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway response to drug Inferred from electronic annotation. Source: Compara skeletal muscle tissue regeneration Inferred from electronic annotation. Source: Compara
Cellular_component	membrane Inferred from electronic annotation. Source: Compara phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphopyruvate hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 434	433	Beta-enolase		PRO_0000134108
Regions
	Region	370 – 373	4	Substrate binding By similarity
Sites
	Active site	210	1	Proton donor By similarity
	Active site	343	1	Proton acceptor By similarity
	Metal binding	245	1	Magnesium By similarity
	Metal binding	293	1	Magnesium By similarity
	Metal binding	318	1	Magnesium By similarity
	Binding site	158	1	Substrate By similarity
	Binding site	167	1	Substrate By similarity
	Binding site	293	1	Substrate By similarity
	Binding site	318	1	Substrate By similarity
	Binding site	394	1	Substrate By similarity
Experimental info
	Sequence conflict	234 – 235	2	AG → NA in AAA37554. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P21550 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A1F757D83709D2B8	FASTA	434	47,025
	10 20 30 40 50 60 MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKARYLGK 70 80 90 100 110 120 GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK 130 140 150 160 170 180 AGAAEKGVPL YRHIADLAGN PDLVLPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE 190 200 210 220 230 240 AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV 250 260 270 280 290 300 VIGMDVAASE FYRNGKYDLD FKSPDDPARH ISGEKLGELY KNFIQNYPVV SIEDPFDQDD 310 320 330 340 350 360 WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA 370 380 390 400 410 420 QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK 430 AVFAGRKFRN PKAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Lamande N., Brosset S., Keller A., Lucas M., Lazar M. Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: BALB/c and Swiss Webster. Tissue: Liver and Skeletal muscle.
[2]	"Beta-enolase is a marker of human myoblast heterogeneity prior to differentiation." Peterson C.A., Cho M., Rastinejad F., Blau H.M. Dev. Biol. 151:626-629(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C3H.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Colon.
[5]	Lubec G., Kang S.U., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 33-50; 104-120; 257-262; 336-358 AND 373-394, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[6]	"Murine muscle-specific enolase: cDNA cloning, sequence, and developmental expression." Lamande N., Mazo A.M., Lucas M., Montarras D., Pinset C., Gros F., Legault-Demare L., Lazar M. Proc. Natl. Acad. Sci. U.S.A. 86:4445-4449(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-434.
[7]	"Activation of the gene encoding the glycolytic enzyme beta-enolase during early myogenesis precedes an increased expression during fetal muscle development." Keller A., Ott M.O., Lamande N., Lucas M., Gros F., Buckingham M., Lazar M. Mech. Dev. 38:41-54(1992) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVATION DURING MYOGENESIS.
[8]	"Differential expression of alpha- and beta-enolase genes during rat heart development and hypertrophy." Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F., Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M. Am. J. Physiol. 269:H1843-H1851(1995) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[9]	"Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins." Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J.-D., Gros F., Lazar M., Keller A. Biochem. J. 323:791-800(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PKM; PGM; CKM; ALDO AND TROPONIN, DEVELOPMENTAL STAGE.
[10]	"Fibre-type distribution and subcellular localisation of alpha and beta enolase in mouse striated muscle." Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C., Lucas M., Chatelet F.-P. Biol. Cell 92:527-535(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[11]	"Differential modulation of alpha, beta and gamma enolase isoforms in regenerating mouse skeletal muscle." Merkulova T., Dehaupas M., Nevers M.C., Creminon C., Alameddine H., Keller A. Eur. J. Biochem. 267:3735-3743(2000) [PubMed] [Europe PMC] [Abstract] Cited for: EXPRESSION REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X61600 Genomic DNA. Translation: CAA43797.1. X57747 mRNA. Translation: CAA40913.1. X62667 mRNA. Translation: CAA44540.1. AK002485 mRNA. Translation: BAB22137.1. BC013460 mRNA. Translation: AAH13460.1. M20745 mRNA. Translation: AAA37554.1.
IPI	IPI00228548.
PIR	NOMSB. S17109.
RefSeq	NP_001129534.1. NM_001136062.2. NP_001263214.1. NM_001276285.1. NP_031959.1. NM_007933.3.
UniGene	Mm.251322.
3D structure databases
ProteinModelPortal	P21550.
SMR	P21550. Positions 1-434.
ModBase	Search...
Protein-protein interaction databases
IntAct	P21550. 2 interactions.
PTM databases
PhosphoSite	P21550.
2D gel databases
SWISS-2DPAGE	P21550.
UCD-2DPAGE	P21550.
Proteomic databases
PaxDb	P21550.
PRIDE	P21550.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000072841; ENSMUSP00000072620; ENSMUSG00000060600. ENSMUST00000108548; ENSMUSP00000104188; ENSMUSG00000060600. ENSMUST00000170716; ENSMUSP00000128714; ENSMUSG00000060600.
GeneID	13808.
KEGG	mmu:13808.
Organism-specific databases
CTD	2027.
MGI	MGI:95395. Eno3.
Phylogenomic databases
eggNOG	COG0148.
GeneTree	ENSGT00550000074560.
HOGENOM	HOG000072174.
HOVERGEN	HBG000067.
InParanoid	P21550.
KO	K01689.
OMA	GELYKNF.
OrthoDB	EOG4T783B.
Enzyme and pathway databases
BRENDA	4.2.1.11. 3474.
UniPathway	UPA00109; UER00187.
Gene expression databases
ArrayExpress	P21550.
Bgee	P21550.
CleanEx	MM_ENO3.
Genevestigator	P21550.
GermOnline	ENSMUSG00000060600. Mus musculus.
Family and domain databases
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
PANTHER	PTHR11902. PTHR11902. 1 hit.
Pfam	PF00113. Enolase_C. 1 hit. PF03952. Enolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF001400. Enolase. 1 hit.
PRINTS	PR00148. ENOLASE.
TIGRFAMs	TIGR01060. eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	284592.
SOURCE	Search...

Entry information

Entry name

ENOB_MOUSE

Accession

Primary (citable) accession number: P21550

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 133 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program